A ribosome-interacting jumbophage protein associates with the phage nucleus to facilitate efficient propagation
1
Issued Date
2025-02-01
Resource Type
ISSN
15537366
eISSN
15537374
Scopus ID
2-s2.0-85219021908
Journal Title
PLoS Pathogens
Volume
21
Issue
2
Rights Holder(s)
SCOPUS
Bibliographic Citation
PLoS Pathogens Vol.21 No.2 (2025)
Suggested Citation
Wannasrichan W., Krobthong S., Morgan C.J., Armbruster E.G., Gerovac M., Yingchutrakul Y., Wongtrakoongate P., Vogel J., Aonbangkhen C., Nonejuie P., Pogliano J., Chaikeeratisak V. A ribosome-interacting jumbophage protein associates with the phage nucleus to facilitate efficient propagation. PLoS Pathogens Vol.21 No.2 (2025). doi:10.1371/journal.ppat.1012936 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/105587
Title
A ribosome-interacting jumbophage protein associates with the phage nucleus to facilitate efficient propagation
Author's Affiliation
Faculty of Science, Mahidol University
Center of Excellence on Petrochemical and Materials Technology
Helmholtz-Institut für RNA-basierte Infektionsforschung
University of California, San Diego
Chulalongkorn University
Julius-Maximilians-Universität Würzburg
Helmholtz Centre for Infection Research (HZI)
Thailand National Center for Genetic Engineering and Biotechnology
Institute of Molecular Biosciences, Mahidol University
Center of Excellence on Petrochemical and Materials Technology
Helmholtz-Institut für RNA-basierte Infektionsforschung
University of California, San Diego
Chulalongkorn University
Julius-Maximilians-Universität Würzburg
Helmholtz Centre for Infection Research (HZI)
Thailand National Center for Genetic Engineering and Biotechnology
Institute of Molecular Biosciences, Mahidol University
Corresponding Author(s)
Other Contributor(s)
Abstract
Bacteriophages must hijack the gene expression machinery of their bacterial host to efficiently replicate. Recently, we have shown that the early-expressed protein gp014 of Pseudomonas nucleus-forming phage phiKZ forms a stable complex with the host ribosomes and modulates the overall protein expression profile during phage infection. Here, we discover a nucleus-forming phage, designated Churi, that is closely related to phiKZ. Churi encodes gp335, a homolog of gp014-phiKZ, which is expressed during the early stages of infection, and its overexpression in bacterial cells interferes with bacterial growth, suggesting its role in phage-host interplay. We predict experimentally that gp335 also interacts with host ribosomal proteins, similar to its homolog gp014-phiKZ, thereby strengthening its involvement in protein translation during phage infection. We further show that GFPtagged gp335 specifically localizes by clustering around the phage nucleus and remains associated with it throughout the infection cycle. The CRISPR-Cas13-mediated deletion of gp335 reveals that the mutant phage fails to replicate efficiently, resulting in an extended latent period. Altogether, our study demonstrates that gp335 is an early-expressed protein of the Chimallivirus Churi that localizes in proximity to the phage nucleus, likely serving a role in localized translation to ensure efficient phage propagation.